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| Title | Structural basis of σ appropriation. |
|---|---|
| Journal, issue, pages | Nucleic Acids Res, Vol. 47, Issue 17, Page 9423-9432, Year 2019 |
| Publish date | Sep 26, 2019 |
 Authors | Jing Shi / Aijia Wen / Minxing Zhao / Linlin You / Yu Zhang / Yu Feng /  |
| PubMed Abstract | Bacteriophage T4 middle promoters are activated through a process called σ appropriation, which requires the concerted effort of two T4-encoded transcription factors: AsiA and MotA. Despite ...Bacteriophage T4 middle promoters are activated through a process called σ appropriation, which requires the concerted effort of two T4-encoded transcription factors: AsiA and MotA. Despite extensive biochemical and genetic analyses, puzzle remains, in part, because of a lack of precise structural information for σ appropriation complex. Here, we report a single-particle cryo-electron microscopy (cryo-EM) structure of an intact σ appropriation complex, comprising AsiA, MotA, Escherichia coli RNA polymerase (RNAP), σ70 and a T4 middle promoter. As expected, AsiA binds to and remodels σ region 4 to prevent its contact with host promoters. Unexpectedly, AsiA undergoes a large conformational change, takes over the job of σ region 4 and provides an anchor point for the upstream double-stranded DNA. Because σ region 4 is conserved among bacteria, other transcription factors may use the same strategy to alter the landscape of transcription immediately. Together, the structure provides a foundation for understanding σ appropriation and transcription activation. |
 External links | Nucleic Acids Res / PubMed:31392983 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.79 Å |
| Structure data | |
| Chemicals |  ChemComp-MG:  ChemComp-ZN: |
| Source |
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 Keywords |  TRANSCRIPTION / RNA polymerase / sigma appropriation / transcription activation / promoter |
